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Reviewed, UniProtKB/Swiss-Prot Q63207 (FA10_RAT)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Coagulation factor X
    EC=3.4.21.6
Alternative name(s):
    Stuart factor
Cleaved into the following 3 chains:
    1- Recommended name:
            Factor X light chain
    2- Recommended name:
            Factor X heavy chain
    3- Recommended name:
            Activated factor Xa heavy chain
Gene names
Name: F10
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

Catalytic activity

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

Subunit structure

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Plasma; synthesized in the liver.

Post-translational modification

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.

N- and O-glycosylated By similarity.

The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) By similarity.

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 4020 By similarity
PRO_0000027804
Chain41 – 482442Coagulation factor X
PRO_0000027805
Chain41 – 180140Factor X light chain By similarity
PRO_0000027806
Chain184 – 482299Factor X heavy chain By similarity
PRO_0000027807
Propeptide184 – 23148Activation peptide By similarity
PRO_0000027808
Chain232 – 482251Activated factor Xa heavy chain By similarity
PRO_0000027809

Regions

Domain41 – 8545Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16541EGF-like 2
Domain232 – 465234Peptidase S1

Sites

Active site2741Charge relay system By similarity
Active site3201Charge relay system By similarity
Active site4171Charge relay system By similarity

Amino acid modifications

Modified residue4614-carboxyglutamate By similarity
Modified residue4714-carboxyglutamate By similarity
Modified residue5414-carboxyglutamate By similarity
Modified residue5614-carboxyglutamate By similarity
Modified residue5914-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6514-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6914-carboxyglutamate By similarity
Modified residue7214-carboxyglutamate By similarity
Modified residue7514-carboxyglutamate By similarity
Modified residue7914-carboxyglutamate By similarity
Modified residue1031(3R)-3-hydroxyaspartate By similarity
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 62 By similarity
Disulfide bond90 ↔ 101 By similarity
Disulfide bond95 ↔ 110 By similarity
Disulfide bond112 ↔ 121 By similarity
Disulfide bond129 ↔ 140 By similarity
Disulfide bond136 ↔ 149 By similarity
Disulfide bond151 ↔ 164 By similarity
Disulfide bond172 ↔ 340Interchain (between light and heavy chains) By similarity
Disulfide bond238 ↔ 243 By similarity
Disulfide bond259 ↔ 275 By similarity
Disulfide bond388 ↔ 402 By similarity
Disulfide bond413 ↔ 441 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q63207-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0284678E3954A698

FASTA48254,265
        10         20         30         40         50         60 
MESPVRLSLL YVVLASLLLP GRSVFINRER ANNVLQRIRR ANSFFEEIKK GNLERECVEE 

        70         80         90        100        110        120 
ICSFEEAREV FEDNEKTTEF WNKYEDGDQC ESSPCQNQGE CRDGLGSYTC TCTEGFEGKN 

       130        140        150        160        170        180 
CELFVRKLCS LDNGDCDQFC REEQNSVVCS CAKGYFLGND GKSCLSTAPF PCGKTNKGRA 

       190        200        210        220        230        240 
KRSVALNTSN SEPDPEDLMP DADILYPTES PSELLNLNKT EPEANSDDVI RIVGGQECKR 

       250        260        270        280        290        300 
GECPWQALLF SDEETDGFCG GTILNEFYIL TAAHCLHQAK RFKVRVGDLN TEQEDGGEMV 

       310        320        330        340        350        360 
HEVDMIIKHN KFQRDTYDFD IAMLRLKTPI TFRENVAPAC LPQKDWAEAT LMTQKTGIVS 

       370        380        390        400        410        420 
GFGRTHEKGR QSKVLKMMEV PYVDRNTCRL STSFSITQNM FCAGYDAKQE DACQGDSGGP 

       430        440        450        460        470        480 
HVTRFKDTYF VTGIVSWGEG CARKGKYGIY TKVTAFLKWI DRSMKARVGP TSETPRLTHP 


PY

« Hide

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References

« Hide 'large scale' references
[1]"Evidence for competition between vitamin K-dependent clotting factors for intracellular processing by the vitamin K-dependent gamma-carboxylase."
Stanton C., Ross R.P., Hutson S., Wallin R.
Thromb. Res. 80:63-73(1995) [PubMed: 8578539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.

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Cross-references

Sequence databases

X79807 mRNA. Translation: CAA56202.1.
BC088151 mRNA. Translation: AAH88151.1.
IPIIPI00206786.
PIREXRT. S49075.
RefSeqNP_058839.1.
UniGeneRn.21393

3D structure databases

HSSPHSSP built from PDB template 1G2L based on UniProtKB P00742.
SMRQ63207. Positions 88-174, 232-473.
ModBaseSearch...

Proteomic databases

PRIDEQ63207.

Genome annotation databases

EnsemblENSRNOG00000033444. Rattus norvegicus. [Contig view]
GeneID29243.
KEGGrno:29243.
NMPDRfig|10116.3.peg.12776.

Organism-specific databases

RGD61850. F10.

Phylogenomic databases

HOVERGENQ63207.

Enzyme and pathway databases

BRENDA3.4.21.6. 248.

Gene expression databases

ArrayExpressQ63207.
GermOnlineENSRNOG00000033444. Rattus norvegicus.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438. EGF_2.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00008. EGF. 2 hits.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00010. EGFBLOOD.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio608522.

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Entry information

Entry nameFA10_RAT
AccessionPrimary (citable) accession number: Q63207
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents